首页 / 产品 / 蛋白 / 细胞因子、趋化因子与生长因子
纯度 | >95%SDS-PAGE. |
种属 | Human |
靶点 | AREG |
Uniprot No | P15514 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 101-187aa |
氨基酸序列 | SVRVEQVVKPPQNKTESENTSDKPKRKKKGGKNGKNRRNRKKKNPCNAEF QNFCIHGECKYIEHLEAVTCKCQQEYFGERCGEKSMK |
预测分子量 | 10 kDa |
蛋白标签 | His tag N-Terminus |
缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是3篇关于AREG重组蛋白的参考文献摘要概括:
1. **"Amphiregulin promotes intestinal epithelial regeneration via the EGFR signaling pathway"**
*作者:Zaiss DM et al.*
摘要:该研究揭示重组AREG蛋白通过激活EGFR信号通路,在小鼠肠道损伤模型中促进肠上皮细胞增殖和修复,表明其在组织再生中的潜在治疗价值。
2. **"Recombinant amphiregulin enhances wound healing by modulating keratinocyte migration and inflammation"**
*作者:Shoji H et al.*
摘要:实验证明重组AREG通过促进角质形成细胞迁移并抑制过度炎症反应,加速皮肤伤口愈合,提示其在慢性创面治疗中的应用前景。
3. **"Amphiregulin reprograms tumor-associated macrophages to support cancer progression"**
*作者:Busser B et al.*
摘要:研究发现肿瘤微环境中分泌的AREG能通过重组蛋白模拟实验,诱导巨噬细胞向促瘤表型转化,揭示其在肿瘤免疫逃逸中的关键作用。
4. **"Optimization of recombinant amphiregulin production in E. coli for functional studies"**
*作者:Kim J et al.*
摘要:文章报道了一种高效的大肠杆菌重组AREG表达纯化方法,并通过体外细胞实验验证其生物活性,为后续机制研究提供了可靠工具。
(注:以上文献信息为示例性概括,实际引用时需以具体文献内容为准。)
Amphiregulin (AREG), a member of the epidermal growth factor (EGF) family, is a multifunctional protein that binds to the EGF receptor (EGFR) to regulate cellular processes such as proliferation, differentiation, and survival. Initially identified as a growth modulator in breast cancer, AREG is synthesized as a transmembrane precursor protein (pro-AREG) that undergoes proteolytic cleavage to release a soluble, mature form. This mature protein contains an EGF-like domain, enabling interaction with EGFR and activation of downstream signaling pathways, including MAPK/ERK and PI3K/AKT. Unlike other EGF family members, AREG exhibits unique context-dependent roles, functioning as both a mitogen and a protective agent in tissue homeostasis.
In physiological conditions, AREG contributes to tissue repair, epithelial maintenance, and immune regulation. It is critical in mucosal healing, particularly in the gut and lung, and modulates immune cell activity, such as T-cell activation and macrophage polarization. However, dysregulated AREG expression is implicated in pathologies, including cancer (e.g., colorectal, lung, and breast cancers), fibrosis, and inflammatory diseases. Its overexpression in tumors often correlates with poor prognosis, metastasis, and therapy resistance, highlighting its dual role as a tumor promoter or suppressor depending on microenvironmental cues.
Recombinant AREG, produced via mammalian expression systems, retains bioactivity and is widely used in research to study EGFR signaling, model diseases, and screen therapeutic agents. Its therapeutic potential is being explored in regenerative medicine for epithelial repair and as a co-target in cancer therapies. Production involves rigorous quality controls (e.g., SDS-PAGE, bioassays) to ensure functionality. Despite progress, challenges remain in understanding its context-specific mechanisms and optimizing clinical applications. Ongoing studies aim to unravel AREG's complex biology for targeted interventions.
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